Molecular and functional characterization of ferritin in abalone Haliotis diversicolor supertexta

Ferritin is an iron storage protein that plays a key role in the processes of physiology and pathology. In the present study, the authors reported the ferritin gene from abalone Haliotis diversicolor supertexta, which we named hds-ferritin. The full-length of hds-ferritin cDNA consisted of 879 bp with an ORF encoding a 171 amino acids. Amino acid sequence analysis revealed that hds-ferritin shared highly homology with other species. Real time PCR and western blot analysis showed that hds-ferritin was distributed ubiquitously in abalone tissues and had the highest expression level in digestive glands, but its transcripts are not modified remarkably by the stimulation with LPS. The recombinant protein was successfully expressed in Escherichia coli BL21 (DE3), and the titre of anti-ferritin antibody was about 1:14 000. The effects of ROS and RNS on ferritin were analyzed in the present study. The results showed that H2O2 played an important role in decreasing hds-ferritin, however NO cation appeared to have a protecting effect on H2O2-medied reduction of hds-ferritin.